ID   KCRB_RABIT              Reviewed;         381 AA.
AC   P00567;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 59.
DE   RecName: Full=Creatine kinase B-type;
DE            EC=2.7.3.2;
DE   AltName: Full=Creatine kinase B chain;
DE   AltName: Full=B-CK;
GN   Name=CKB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85190487; PubMed=3857581;
RA   Pickering L., Pang H., Biemann K., Munro H., Schimmel P.;
RT   "Two tissue-specific isozymes of creatine kinase have closely matched
RT   amino acid sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC       the major form in skeletal muscle and myocardium, MB existing in
CC       myocardium, and BB existing in many tissues, especially brain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; M11306; AAA31201.1; -; mRNA.
DR   PIR; A00678; KIRBCB.
DR   RefSeq; NP_001075730.1; -.
DR   UniGene; Ocu.3366; -.
DR   HSSP; P05122; 1QH4.
DR   SMR; P00567; 2-381.
DR   Ensembl; ENSOCUG00000008818; Oryctolagus cuniculus.
DR   GeneID; 100009085; -.
DR   HOVERGEN; P00567; -.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0005515; F:protein binding; ISS:AgBase.
DR   GO; GO:0007420; P:brain development; ISS:AgBase.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; ISS:AgBase.
DR   InterPro; IPR000749; ATP-gua_Ptrans.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   PROSITE; PS00112; GUANIDO_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       Creatine kinase B-type.
FT                                /FTId=PRO_0000211969.
FT   NP_BIND     128    132       ATP (By similarity).
FT   NP_BIND     320    325       ATP (By similarity).
FT   BINDING     191    191       ATP (By similarity).
FT   BINDING     236    236       ATP (By similarity).
FT   BINDING     292    292       ATP (By similarity).
FT   BINDING     335    335       ATP (By similarity).
FT   MOD_RES     125    125       Phosphotyrosine (By similarity).
FT   MOD_RES     164    164       Phosphoserine (By similarity).
SQ   SEQUENCE   381 AA;  42663 MW;  0001F0FF3A1F3F40 CRC64;
     MPFSNTHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPEMDA ELRAKSTPSG FTLDDVIQTG
     VDNPGHPFIM TVGCVAGDEE SYEAFKELFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD
     LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAVEKLAVE ALSSLDGDLA GRYYALKSMT
     EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
     QKGGNMKEVF TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
     HLGQHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
     IEMEQRLEQG QAIDDLMPAQ K
//